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Database: UniProt
Entry: G1S8X0_NOMLE
LinkDB: G1S8X0_NOMLE
Original site: G1S8X0_NOMLE 
ID   G1S8X0_NOMLE            Unreviewed;      1591 AA.
AC   G1S8X0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1S {ECO:0000313|Ensembl:ENSNLEP00000021959};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates
OS   leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hylobatidae; Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000021959};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000021959}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000021959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. Binding of
CC       calmodulin or CABP1 at the same regulatory sites results in an
CC       opposit effects on the channel function.
CC       {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSNLEP00000021959}.
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DR   EMBL; ADFV01023222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01023223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01023224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01023225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01023226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01023227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 61853.ENSNLEP00000021959; -.
DR   Ensembl; ENSNLET00000023071; ENSNLEP00000021959; ENSNLEG00000018075.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; G1S8X0; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000001073; Unplaced.
DR   GO; GO:0031674; C:I band; IEA:Ensembl.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0006936; P:muscle contraction; IEA:Ensembl.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005450; VDCC_L_a1ssu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF190; PTHR10037:SF190; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01634; LVDCCALPHA1S.
DR   SMART; SM01062; Ca_chan_IQ; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU003808};
KW   Calcium channel {ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|RuleBase:RU003808};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001073};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM      6     22       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     42     62       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     74     95       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    146    168       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    228    249       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    261    283       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    383    400       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    420    438       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    512    531       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    584    611       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    745    768       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    823    846       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    867    887       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    992   1018       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1072   1090       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1102   1120       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1216   1234       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1307   1331       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1465   1498       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1591 AA;  182086 MW;  7C90B5B55B1F5AF5 CRC64;
     RPFETIILLT IFANCVALAV YLPMPEDDNN SLNLSLEKLE YFFLIVFSIE AAMKIIAYGF
     LFHQDAYLRS GWNVLDFTIV FLGVFTVILE QVNVIQSHTA PMSSKGAGLD VKALRAFRVL
     RPLRLVSGVP SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFTG
     TDIVATVENE EPSPCARTGS GRRCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT
     MEGWTDVLYW VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF
     QKLREKQQLD EDLRGYMSWI TQGEVMDVED FREGKLSLDE GGSDTESLYE IAGLNKIIQF
     IRHWRQWNRI FRWKCHDIVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL TRLQDIANRV
     LLSLFTVEML IKMYGLGLRQ YFMSIFNRFD CFVVCSGILE ILLVESGAMT PLGISVLRCI
     RLLRIFKITK YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT
     EVRRSNFDNF PQALISVFQV LTGEDWTSMM YNGIMAYGGP SYPGMLVCIY FIILFVCGNY
     ILLNVFLAIA VDNLAEAESL TSAQKAKAEE RKRRKMSKGL PEKSEEEKST MAKKLEQKPK
     GEGIPTTAKL KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPLSPRPRP LAELQLKEKA
     VPIPEASSFF IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRADSMRNQ
     ILKHFDIGFT SVFTVEIVLK MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI
     SVVKILRVLR VLRPLRAINR AKGLKRVVQC MFVAIXXXXX XXXXXXXXXX XXXXIGVQLF
     KGKFFRCTDL SKMTEEECRG YYYVYKDGDP TQIELRHREW VHSDFHFDNV LSAMMSLFTV
     STFEGWPQLL YKAIDSNEED MGPIYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE
     QGETEYKNCE LNKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYIVTSSYF EYLMFALIML
     NTICLGMQHY NQSEQMNHIS DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV
     IGSIIDVILS EIDTFLASSG GLYCLGGGCG NIDPDESARI SSAFFRLFRV MRLIKLLSRA
     EGVRTLLWTF IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI NRNNNFQTFP
     QAVLLLFRCA TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF
     LVINLFVAVI MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ
     PPLGFGKFCP HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL
     RAIIKKIWKR TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK
     DVVQIQAGLR TIEEEAAPEI RRTISDLAAE EELERAMVEA AMEEGIFRRT GGLFGQVDNF
     LERTNSLPPV MANQRPLQFA EIEMEEMESP V
//
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